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CATH Superfamily 3.90.55.10

Dimethylsulfoxide Reductase, domain 3

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Dimethylsulfoxide Reductase, domain 3
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Biotin sulfoxide reductase 2

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
L-methionine (S)-S-oxide reductase. [EC: 1.8.4.13]
L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin.
  • The reaction occurs in the opposite direction to that given above.
  • Dithiothreitol can replace reduced thioredoxin.
  • L-methionine (R)-S-oxide is not a substrate (see EC 1.8.4.14).
  • Formerly EC 1.8.4.5.
 72 A0A070USH1 A0A070USH1 A0A070USH1 A0A070USH1 A0A070USH1 A0A070USH1 A0A070USH1 A0A070USH1 A0A0E1M4Q2 A0A0E1M4Q2
(62 more...)
Trimethylamine-N-oxide reductase. [EC: 1.7.2.3]
Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+).
  • Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor.
  • The reductant is a membrane-bound multiheme cytochrome c.
  • Also reduces dimethyl sulfoxide to dimethyl sulfide.
 45 A0A0F6C5G6 A0A0F6C5G6 A0A0F6C5G6 A0A0F6C5G6 A0A0F6C5G6 A0A0F6C5G6 A0A0H3PI48 A0A0H3PI48 A0A0H3PI48 A0A0H3PI48
(35 more...)